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Thiolate-bridged Complex
Transition metal thiolate complexes are metal complexes containing thiolate ligands. Thiolates are ligands that can be classified as soft Lewis bases. Therefore, thiolate ligands coordinate most strongly to metals that behave as soft Lewis acids as opposed to those that behave as hard Lewis acids. Most complexes contain other ligands in addition to thiolate, but many homoleptic complexes are known with only thiolate ligands. The amino acid cysteine has a thiol functional group, consequently many cofactors in proteins and enzymes feature cysteinate-metal cofactors. Synthesis Metal thiolate complexes are commonly prepared by reactions of metal complexes with thiols (RSH), thiolates (RS−), and disulfides (R2S2). The salt metathesis reaction route is common. In this method, an alkali metal thiolate is treated with a transition metal halide to produce an alkali metal halide and the metal thiolate complex: :LiSC6H5 + CuI → Cu(SC6H5) + LiI The thiol ligand can also effe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metal Complex
A coordination complex consists of a central atom or ion, which is usually metallic and is called the ''coordination centre'', and a surrounding array of bound molecules or ions, that are in turn known as ''ligands'' or complexing agents. Many metal-containing compounds, especially those that include transition metals (elements like titanium that belong to the Periodic Table's d-block), are coordination complexes. Nomenclature and terminology Coordination complexes are so pervasive that their structures and reactions are described in many ways, sometimes confusingly. The atom within a ligand that is bonded to the central metal atom or ion is called the donor atom. In a typical complex, a metal ion is bonded to several donor atoms, which can be the same or different. A polydentate (multiple bonded) ligand is a molecule or ion that bonds to the central atom through several of the ligand's atoms; ligands with 2, 3, 4 or even 6 bonds to the central atom are common. These compl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Biochemistry
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research. Voet (2005), p. 3. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, Karp (2009), p. 2. in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function.Miller (2012). p. 62. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenomena.Ast ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Plastocyanin Copper Binding
Plastocyanin is a copper-containing protein that mediates electron-transfer. It is found in a variety of plants, where it participates in photosynthesis. The protein is a prototype of the blue copper proteins, a family of intensely blue-colored metalloproteins. Specifically, it falls into the group of small type I blue copper proteins called "cupredoxins". Function In photosynthesis, plastocyanin functions as an electron transfer agent between cytochrome f of the cytochrome ''b''6''f'' complex from photosystem II and P700+ from photosystem I. Cytochrome ''b''6''f'' complex and P700+ are both membrane-bound proteins with exposed residues on the lumen-side of the thylakoid membrane of chloroplasts. Cytochrome f acts as an electron donor while P700+ accepts electrons from reduced plastocyanin. Structure The copper site in plastocyanin, with the four amino acids that bind the metal labelled. Plastocyanin was the first of the blue copper proteins to be characterised by X- ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molybdopterin
Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopterin are: MPT and pyranopterin-dithiolate. The nomenclature for this biomolecule can be confusing: Molybdopterin itself contains no molybdenum; rather, this is the name of the ligand (a '' pterin'') that will bind the active metal. After molybdopterin is eventually complexed with molybdenum, the complete ligand is usually called molybdenum cofactor. Molybdopterin consists of a pyranopterin, a complex heterocycle featuring a pyran fused to a pterin ring. In addition, the pyran ring features two thiolates, which serve as ligands in molybdo- and tungstoenzymes. In some cases, the alkyl phosphate group is replaced by an alkyl diphosphate nucleotide. Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate reductase. The only molybdenum-containing enzymes that do not feature molybdo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Liver Alcohol Dehydrogenase
Alcohol dehydrogenases (ADH) () are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalysis, catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Evolution Genetic evidence from comparisons of multiple organisms showed that a glutathione-dependent formaldehyde dehydrogenase, identical to a ADH5, class III alcohol dehydrogenase (ADH-3/ADH5), is presumed to be the ancestral enzyme for the entire ADH family. Early on in evolution, an effective method for eliminating both endogenous and exogenou ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
